|
Name |
Accession |
Description |
Interval |
E-value |
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
1-296 |
3.19e-158 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 442.53 E-value: 3.19e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 1 MAQIIDGKAIAQEVRTQLAHELKGMEAAGYPkPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQ 80
Cdd:COG0190 2 MAQILDGKAVAAEIREELKERVAALKAKGIT-PGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 81 LIADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRN 160
Cdd:COG0190 81 LIDELNADPSVHGILVQLPLPKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 161 AVVVGRSKNVSLPMAILLhadgkyaTKAmDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVG 240
Cdd:COG0190 161 AVVVGRSNIVGKPLALLL-------LRR-NATVTVCHSRT--KDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVG 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136818 241 INRIKDEstgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQ 296
Cdd:COG0190 231 INRVEDG-----KLVGDVDFESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQ 281
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-300 |
1.31e-125 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 360.00 E-value: 1.31e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 2 AQIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQL 81
Cdd:PRK10792 3 AKIIDGKTIAQQVRSEVAQKVQARVAAGLRAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELLAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 82 IADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNA 161
Cdd:PRK10792 83 IDELNADPTIDGILVQLPLPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGLNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 162 VVVGRSKNVSLPMAI-LLHAdgkyatkamDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVG 240
Cdd:PRK10792 163 VVVGASNIVGRPMSLeLLLA---------GCTVTVCHRFT--KNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 241 INRIKDEstgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARkQFDDR 300
Cdd:PRK10792 232 INRLEDG-----KLVGDVEFETAAERASWITPVPGGVGPMTVATLLENTLQACE-EYHDP 285
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-296 |
5.55e-125 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 358.17 E-value: 5.55e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 1 MAQIIDGKAIAQEVRTQLAHELKGMEAAGYpKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQ 80
Cdd:PRK14190 2 MAVIIDGKEVAKEKREQLKEEVVKLKEQGI-VPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 81 LIADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRN 160
Cdd:PRK14190 81 LIDRLNADPRINGILVQLPLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 161 AVVVGRSKNVSLPMAILLHADgkyatkamDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVG 240
Cdd:PRK14190 161 VVVVGRSNIVGKPVGQLLLNE--------NATVTYCHSKT--KNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVG 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136818 241 INRIKDEstgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQ 296
Cdd:PRK14190 231 VNRLENG-----KLCGDVDFDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRA 281
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-296 |
4.97e-124 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 356.19 E-value: 4.97e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 1 MAQIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQ 80
Cdd:PRK14188 1 MATIIDGKAFAADVRATVAAEVARLKAAHGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 81 LIADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRN 160
Cdd:PRK14188 81 LIARLNADPAIHGILVQLPLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 161 AVVVGRSKNVSLPMAILLHADgkyatkamDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVG 240
Cdd:PRK14188 161 AVVIGRSNLVGKPMAQLLLAA--------NATVTIAHSRT--RDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVG 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17136818 241 INRI--KDESTGQFKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQ 296
Cdd:PRK14188 231 INRIpaPEKGEGKTRLVGDVAFAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACRA 288
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
2-295 |
2.05e-113 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 328.96 E-value: 2.05e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 2 AQIIDGKAIAQEVRTQLAHELKGMEAAGYpKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQL 81
Cdd:PRK14189 3 AQLIDGNALSKQLRAEAAQRAAALTARGH-QPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 82 IADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNA 161
Cdd:PRK14189 82 IDELNRDPKIHGILVQLPLPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 162 VVVGRSKNVSLPMAILLHADGkyatkamdATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGI 241
Cdd:PRK14189 162 VVIGRSNIVGKPMAMLLLQAG--------ATVTICHSKT--RDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17136818 242 NRIKDEstgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARK 295
Cdd:PRK14189 232 NRDDAG-----KLCGDVDFAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAER 280
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-297 |
7.36e-112 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 325.48 E-value: 7.36e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 1 MAQIIDGKAIAQEVRTQLAHEL-KGMEAAGYPkPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELL 79
Cdd:PRK14186 1 MALILDGKALAAEIEQRLQAQIeSNLPKAGRP-PGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 80 QLIADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGR 159
Cdd:PRK14186 80 ALIAQLNQDERVDGILLQLPLPKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 160 NAVVVGRSKNVSLPMAILLhadgkyatKAMDATVTICHRYTPpkELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDV 239
Cdd:PRK14186 160 KAVVVGRSILVGKPLALML--------LAANATVTIAHSRTQ--DLASITREADILVAAAGRPNLIGAEMVKPGAVVVDV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17136818 240 GINRIKDeSTGQFKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQF 297
Cdd:PRK14186 230 GIHRLPS-SDGKTRLCGDVDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLSWQKRH 286
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
3-296 |
1.30e-109 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 319.41 E-value: 1.30e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 3 QIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQLI 82
Cdd:PRK14184 2 LLLDGKATAATIREELKTEVAALTARHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 83 ADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNAV 162
Cdd:PRK14184 82 AELNARPDIDGILLQLPLPKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 163 VVGRSKNVSLPMAILLHADGKYAtkamDATVTICHRYTPpkELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGIN 242
Cdd:PRK14184 162 VVGRSNIVGKPLALMLGAPGKFA----NATVTVCHSRTP--DLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGIN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17136818 243 RIKDestgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQ 296
Cdd:PRK14184 236 RTDD------GLVGDCDFEGLSDVASAITPVPGGVGPMTIAQLLVNTVQSWKER 283
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-296 |
2.86e-109 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 318.63 E-value: 2.86e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 3 QIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQLI 82
Cdd:PRK14191 2 VLLDGKALSYKIEKDLKNKIQILTAQTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 83 ADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNAV 162
Cdd:PRK14191 82 KDLNTDQNIDGILVQLPLPRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 163 VVGRSKNVSLPMAILLHADGkyatkamdATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGIN 242
Cdd:PRK14191 162 IIGASNIVGKPLAMLMLNAG--------ASVSVCHILT--KDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGIN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17136818 243 RIKDEstgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQ 296
Cdd:PRK14191 232 RLNDG-----RLVGDVDFENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKR 280
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
2-300 |
2.08e-100 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 295.97 E-value: 2.08e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 2 AQIIDGKAIAQEVRTQLAHELKGMEAAgypkPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQL 81
Cdd:PRK14173 3 ARELSGPPAAEAVYAELRARLAKLPFV----PHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 82 IADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNA 161
Cdd:PRK14173 79 IARLNADPEVDGILVQLPLPPHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 162 VVVGRSKNVSLPMA-ILLHAdgkyatkamDATVTICHRYTPpkELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVG 240
Cdd:PRK14173 159 VVVGRSNIVGKPLAaLLLRE---------DATVTLAHSKTQ--DLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVG 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 241 INRIKDEStGQFKLVGDVDfEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQFDDR 300
Cdd:PRK14173 228 INRVGGNG-GRDILTGDVH-PEVAEVAGALTPVPGGVGPMTVAMLMANTVIAALRRRGGR 285
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
3-295 |
2.10e-100 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 296.35 E-value: 2.10e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 3 QIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQLI 82
Cdd:PRK14174 2 LIIDGKKVSLDLKNELKTRVEAYRAKTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 83 ADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDM--EANIPATPLGVKRLLEHMKIETLGRN 160
Cdd:PRK14174 82 EDLNNDPDVHGILVQQPLPKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGHldKCFVSCTPYGILELLGRYNIETKGKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 161 AVVVGRSKNVSLPMAILLHADgkyaTKAMDATVTICHRYTPpkELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVG 240
Cdd:PRK14174 162 CVVVGRSNIVGKPMANLMLQK----LKESNCTVTICHSATK--DIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136818 241 INRIKDESTGQ-FKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARK 295
Cdd:PRK14174 236 INRIEDPSTKSgYRLVGDVDYEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFER 291
|
|
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-296 |
9.32e-99 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 291.92 E-value: 9.32e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 1 MAQIIDGKAIAQEVRTQLAHELKGMEAAGYpKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQ 80
Cdd:PRK14193 2 TAIILDGKATADEIKADLAERVAALKEKGI-TPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 81 LIADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRN 160
Cdd:PRK14193 81 VIDELNADPACTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 161 AVVVGRSKNVSLPMAILLhadgkyATKAMDATVTICHryTPPKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVG 240
Cdd:PRK14193 161 VVVIGRGVTVGRPIGLLL------TRRSENATVTLCH--TGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136818 241 INRIKDestgqFKLVGDVDfEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQ 296
Cdd:PRK14193 233 VSRAGD-----GKLVGDVH-PDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERR 282
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
1-296 |
1.31e-98 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 291.27 E-value: 1.31e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 1 MAQIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQ 80
Cdd:PRK14179 1 MTEIIDGKALAQKMQAELAEKVAKLKEEKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 81 LIADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRN 160
Cdd:PRK14179 81 LIERYNQDPTWHGILVQLPLPKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 161 AVVVGRSKNVSLPMAILLHADgkyatkamDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVG 240
Cdd:PRK14179 161 AVVIGRSNIVGKPMAQLLLDK--------NATVTLTHSRT--RNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVG 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136818 241 INRikDESTgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQ 296
Cdd:PRK14179 231 MNR--DENG---KLIGDVDFDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALRS 281
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-297 |
1.80e-97 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 289.04 E-value: 1.80e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 3 QIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQLI 82
Cdd:PRK14185 2 QLIDGKAISAQIKQEIAAEVAEIVAKGGKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 83 ADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNAV 162
Cdd:PRK14185 82 RELNQDDDVDGFIVQLPLPKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 163 VVGRSKNVSLPMAILLHADGKYAtkamDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGIN 242
Cdd:PRK14185 162 VLGRSNIVGKPMAQLMMQKAYPG----DCTVTVCHSRS--KNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTT 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136818 243 RIKDESTGQ-FKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQF 297
Cdd:PRK14185 236 RVPDATRKSgFKLTGDVKFDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAI 291
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-298 |
2.62e-95 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 283.07 E-value: 2.62e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 4 IIDGKAIAQEVRTQLAHELKGMEAAGYpKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQLIA 83
Cdd:PRK14166 3 LLDGKALSAKIKEELKEKNQFLKSKGI-ESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 84 DLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEAN-IPATPLGVKRLLEHMKIETLGRNAV 162
Cdd:PRK14166 82 TLNHDDSVHGILVQLPLPDHICKDLILESIISSKDVDGFHPINVGYLNLGLESGfLPCTPLGVMKLLKAYEIDLEGKDAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 163 VVGRSKNVSLPMAILLHADGkyatkamdATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGIN 242
Cdd:PRK14166 162 IIGASNIVGRPMATMLLNAG--------ATVSVCHIKT--KDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGIN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136818 243 RIKDEstgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQFD 298
Cdd:PRK14166 232 RLESG-----KIVGDVDFEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKNRLN 282
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-298 |
3.41e-95 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 283.21 E-value: 3.41e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 1 MAQIIDGKAIAQEVRTQLAHELKGMEAAGYpKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQ 80
Cdd:PRK14167 1 MTEIIDGNAVAAQIRDDLTDAIETLEDAGV-TPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 81 LIADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRN 160
Cdd:PRK14167 80 TIDELNADEDVHGILVQMPVPDHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 161 AVVVGRSKNVSLPMAILL--HADGKyatkamDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVID 238
Cdd:PRK14167 160 VVVVGRSDIVGKPMANLLiqKADGG------NATVTVCHSRT--DDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVID 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 239 VGINRIKDESTGQFKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQFD 298
Cdd:PRK14167 232 VGINRVDADTEKGYELVGDVEFESAKEKASAITPVPGGVGPMTRAMLLYNTVKAASLQEG 291
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
3-294 |
1.30e-93 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 278.64 E-value: 1.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 3 QIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQLI 82
Cdd:PRK14183 2 QILDGKALSDKIKENVKKEVDELKLVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 83 ADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNAV 162
Cdd:PRK14183 82 AMMNNNPNIDGILVQLPLPKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 163 VVGRSKNVSLPMAILLHADGkyatkamdATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGIN 242
Cdd:PRK14183 162 VVGASNIVGKPMAALLLNAN--------ATVDICHIFT--KDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGIN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17136818 243 RIKDEstgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAAR 294
Cdd:PRK14183 232 RTEDG-----RLVGDVDFENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAK 278
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-296 |
2.92e-93 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 278.65 E-value: 2.92e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 2 AQIIDGKAIAQEVRTQLAHELKGMEAAGYpKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQL 81
Cdd:PRK14194 4 AKLIDGKAAAARVLAQVREDVRTLKAAGI-EPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 82 IADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNA 161
Cdd:PRK14194 83 IAELNADPSVNGILLQLPLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 162 VVVGRSKNVSLPMAILLhadgkyaTKAmDATVTICH-RYTPPKELarhCRQADIIVVAVGKPGLITKDMVKPGACVIDVG 240
Cdd:PRK14194 163 VVIGRSNIVGKPMAALL-------LQA-HCSVTVVHsRSTDAKAL---CRQADIVVAAVGRPRLIDADWLKPGAVVIDVG 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136818 241 INRIKDEstGQFKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQ 296
Cdd:PRK14194 232 INRIDDD--GRSRLVGDVDFDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAARLQ 285
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
2-295 |
4.86e-93 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 279.97 E-value: 4.86e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 2 AQIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQL 81
Cdd:PLN02616 73 AKVIDGKAVAKKIRDEITIEVSRMKESIGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 82 IADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEAN--IPATPLGVKRLLEHMKIETLGR 159
Cdd:PLN02616 153 ISGFNNDPSVHGILVQLPLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPlfVPCTPKGCIELLHRYNVEIKGK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 160 NAVVVGRSKNVSLPMAILLHADgkyatkamDATVTICH-RYTPPKELARHcrqADIIVVAVGKPGLITKDMVKPGACVID 238
Cdd:PLN02616 233 RAVVIGRSNIVGMPAALLLQRE--------DATVSIVHsRTKNPEEITRE---ADIIISAVGQPNMVRGSWIKPGAVVID 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17136818 239 VGINRIKDESTGQ-FKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARK 295
Cdd:PLN02616 302 VGINPVEDASSPRgYRLVGDVCYEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKR 359
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
1-297 |
7.78e-93 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 277.16 E-value: 7.78e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 1 MAQIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQ 80
Cdd:PLN02516 8 VAQIIDGKAIAKAIRSEIAEEVAQLSEKHGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 81 LIADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDME--ANIPATPLGVKRLLEHMKIETLG 158
Cdd:PLN02516 88 KVHELNANPDVHGILVQLPLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKGRepLFLPCTPKGCLELLSRSGIPIKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 159 RNAVVVGRSKNVSLPMAILLhadgkyaTKAmDATVTICHRYTPPKElaRHCRQADIIVVAVGKPGLITKDMVKPGACVID 238
Cdd:PLN02516 168 KKAVVVGRSNIVGLPVSLLL-------LKA-DATVTVVHSRTPDPE--SIVREADIVIAAAGQAMMIKGDWIKPGAAVID 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 239 VGINRIKDESTGQ-FKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQF 297
Cdd:PLN02516 238 VGTNAVSDPSKKSgYRLVGDVDFAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKRVF 297
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-295 |
6.00e-92 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 274.76 E-value: 6.00e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 4 IIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQLIA 83
Cdd:PRK14176 10 IIDGKALAKKIEAEVRSGVERLKSNRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 84 DLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNAVV 163
Cdd:PRK14176 90 SLNKRKDVHGILLQLPLPKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 164 VGRSKNVSLPMAILLhadgkyatKAMDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGINR 243
Cdd:PRK14176 170 VGHSNVVGKPMAAML--------LNRNATVSVCHVFT--DDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17136818 244 IKDestgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARK 295
Cdd:PRK14176 240 EED------KVYGDVDFENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEK 285
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-294 |
3.16e-88 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 265.59 E-value: 3.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 2 AQIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQL 81
Cdd:PRK14168 3 AKIIKGTEIREEILEEIRGEVAELKEKYGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELLAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 82 IADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTAL--DMEANIPATPLGVKRLLEHMKIETLGR 159
Cdd:PRK14168 83 IDKYNNDDSIHGILVQLPLPKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIggDEVKFLPCTPAGIQEMLVRSGVETSGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 160 NAVVVGRSKNVSLPMAILLHADGKYAtkamDATVTICHryTPPKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDV 239
Cdd:PRK14168 163 EVVVVGRSNIVGKPIANMMTQKGPGA----NATVTIVH--TRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136818 240 GINRI-KDESTGQFKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAAR 294
Cdd:PRK14168 237 GVNRVgTNESTGKAILSGDVDFDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAK 292
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-294 |
3.20e-87 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 262.54 E-value: 3.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 2 AQIIDGKAIAQEVRTQLAHELKGMEAAGYpKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQL 81
Cdd:PRK14175 3 AKILDGKQIAKDYRQGLQDQVEALKEKGF-TPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 82 IADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNA 161
Cdd:PRK14175 82 LNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 162 VVVGRSKNVSLPMAILLhadgkyatKAMDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGi 241
Cdd:PRK14175 162 VVIGRSHIVGQPVSKLL--------LQKNASVTILHSRS--KDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVG- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17136818 242 nRIKDESTgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAAR 294
Cdd:PRK14175 231 -NTPDENG---KLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEK 279
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
2-298 |
8.22e-87 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 263.74 E-value: 8.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 2 AQIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQL 81
Cdd:PLN02897 56 TVVIDGNVIAEEIRTKIASEVRKMKKAVGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILSA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 82 IADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEAN--IPATPLGVKRLLEHMKIETLGR 159
Cdd:PLN02897 136 LRKFNEDTSIHGILVQLPLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPlfVSCTPKGCVELLIRSGVEIAGK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 160 NAVVVGRSKNVSLPMAILLhadgkyatKAMDATVTICHRYTP-PKELArhcRQADIIVVAVGKPGLITKDMVKPGACVID 238
Cdd:PLN02897 216 NAVVIGRSNIVGLPMSLLL--------QRHDATVSTVHAFTKdPEQIT---RKADIVIAAAGIPNLVRGSWLKPGAVVID 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136818 239 VGINRIKDESTG-QFKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQFD 298
Cdd:PLN02897 285 VGTTPVEDSSCEfGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRIFL 345
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
123-297 |
2.17e-85 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 253.16 E-value: 2.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 123 NEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNAVVVGRSKNVSLPMAILLHADgkyatkamDATVTICHRYTpp 202
Cdd:pfam02882 1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--------NATVTVCHSKT-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 203 KELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGINRIKDestgqFKLVGDVDFEEVRQVAGHITPVPGGVGPMTV 282
Cdd:pfam02882 71 KDLAEITREADIVVVAVGKPELIKADWIKPGAVVIDVGINRVGN-----GKLVGDVDFENVKEKASAITPVPGGVGPMTV 145
|
170
....*....|....*
gi 17136818 283 AMLMHNTLKAARKQF 297
Cdd:pfam02882 146 AMLLQNTVEAAKRQL 160
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-296 |
1.24e-84 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 255.54 E-value: 1.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 4 IIDGKAIAqEVRTQLAHElKGMEAAGYPKphLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQLIA 83
Cdd:PRK14178 2 ILDGKAVS-EKRLELLKE-EIIESGLYPR--LATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 84 DLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNAVV 163
Cdd:PRK14178 78 RLNEDPDINGILVQLPLPKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 164 VGRSKNVSLPMA-ILLHAdgkyatkamDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGIN 242
Cdd:PRK14178 158 VGRSIDVGRPMAaLLLNA---------DATVTICHSKT--ENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGIN 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17136818 243 RIkdestgQFKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQ 296
Cdd:PRK14178 227 QV------NGKLCGDVDFDAVKEIAGAITPVPGGVGPMTIATLMENTFDAAKMR 274
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-296 |
1.47e-84 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 255.91 E-value: 1.47e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 1 MAQIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQ 80
Cdd:PRK14187 1 ETNIIDGKKIANDITEILATCIDDLKRQHNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 81 LIADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEAN--IPATPLGVKRLLEHMKIETLG 158
Cdd:PRK14187 81 KINELNNDDSVHGILVQLPVPNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQKKNclIPCTPKGCLYLIKTITRNLSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 159 RNAVVVGRSKNVSLPMAILLHADgkyatkamDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVID 238
Cdd:PRK14187 161 SDAVVIGRSNIVGKPMACLLLGE--------NCTVTTVHSAT--RDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVID 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17136818 239 VGINRIKDEstGQFKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQ 296
Cdd:PRK14187 231 VGINSIEEG--GVKKFVGDVDFAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAACNQ 286
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-296 |
2.45e-84 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 255.25 E-value: 2.45e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 2 AQIIDGKAIAQEVRTQLAHELKGMEAAGYpKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQL 81
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQDV-TPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 82 IADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNA 161
Cdd:PRK14169 80 VAELNHDPDVDAILVQLPLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 162 VVVGRSKNVSLPMAILLhadgkyatKAMDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGI 241
Cdd:PRK14169 160 VIVGRSNIVGRPLAGLM--------VNHDATVTIAHSKT--RNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGI 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17136818 242 NRIKDEstgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQ 296
Cdd:PRK14169 230 SRGADG-----KLLGDVDEAAVAPIASAITPVPGGVGPMTIASLMAQTVTLAKRR 279
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
115-294 |
1.04e-83 |
|
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding domain of the Methylene-Tetrahydrofolate Dehydrogenase/cyclohydrolase (m-THF DH/cyclohydrolase) bifunctional enzyme. Tetrahydrofolate is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofucntional DH, as well as bifunctional m-THF m-THF DHm-THF DHDH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains the bifunctional DH/cyclohydrolase. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains.
Pssm-ID: 133448 Cd Length: 168 Bit Score: 249.39 E-value: 1.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 115 VDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNAVVVGRSKNVSLPMAILLhadgkyatKAMDATVT 194
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALL--------LNRNATVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 195 ICHRYTPpkELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGINRIKDESTGqfKLVGDVDFEEVRQVAGHITPVP 274
Cdd:cd01080 73 VCHSKTK--NLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVPDKSGG--KLVGDVDFESAKEKASAITPVP 148
|
170 180
....*....|....*....|
gi 17136818 275 GGVGPMTVAMLMHNTLKAAR 294
Cdd:cd01080 149 GGVGPMTVAMLMKNTVEAAK 168
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-296 |
2.91e-81 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 247.07 E-value: 2.91e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 1 MAQIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQ 80
Cdd:PRK14192 2 MALVLDGKALAKQIEEELSVRVEALKAKTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 81 LIADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRN 160
Cdd:PRK14192 82 KIEELNANPDVHGILLQHPVPAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 161 AVVVGRSKNVSLPMA-ILLHAdgkyatkamDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDV 239
Cdd:PRK14192 162 AVVVGRSAILGKPMAmMLLNA---------NATVTICHSRT--QNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDA 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 17136818 240 GINRIKDEStgqfklVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQ 296
Cdd:PRK14192 231 GFHPRDGGG------VGDIELQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKA 281
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-292 |
1.67e-79 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 242.76 E-value: 1.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 1 MAQIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQ 80
Cdd:PRK14172 1 MGQIINGKEVALKIKEEIKNFVEERKENGLSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 81 LIADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRN 160
Cdd:PRK14172 81 EIEELNKDNNVHGIMLQLPLPKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 161 AVVVGRSKNVSLPMAILLHADgkyatkamDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVG 240
Cdd:PRK14172 161 VVVIGRSNIVGKPVAQLLLNE--------NATVTICHSKT--KNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVG 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17136818 241 InrikdeSTGQFKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKA 292
Cdd:PRK14172 231 T------SSVNGKITGDVNFDKVIDKASYITPVPGGVGSLTTTLLIKNVCEA 276
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-297 |
1.82e-79 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 242.57 E-value: 1.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 4 IIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQLIA 83
Cdd:PRK14177 5 LLDGKKLSEKIRNEIRETIEERKTKNKRIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 84 DLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNAVV 163
Cdd:PRK14177 85 KLNLDPNVDGILLQHPVPSQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKNAVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 164 VGRSKNVSLPMAILLhadgkyatKAMDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGINr 243
Cdd:PRK14177 165 VGRSPILGKPMAMLL--------TEMNATVTLCHSKT--QNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17136818 244 ikdesTGQfklVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQF 297
Cdd:PRK14177 234 -----PGN---VGDIEISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKEHF 279
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-295 |
2.27e-78 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 239.92 E-value: 2.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 4 IIDGKAIAQEVRTQLAHELKGMEAAGYpKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQLIA 83
Cdd:PRK14182 3 LIDGKQIAAKVKGEVATEVRALAARGV-QTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 84 DLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANI-PATPLGVKRLLEHMKIETLGRNAV 162
Cdd:PRK14182 82 RLNADPAVHGILVQLPLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGVPrPCTPAGVMRMLDEARVDPKGKRAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 163 VVGRSKNVSLPMAILLhadgkyatKAMDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGIN 242
Cdd:PRK14182 162 VVGRSNIVGKPMAMML--------LERHATVTIAHSRT--ADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17136818 243 RIKDEstgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARK 295
Cdd:PRK14182 232 RLADG-----KLVGDVEFAAAAARASAITPVPGGVGPMTRAMLLVNTVELAKR 279
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-295 |
8.76e-77 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 235.69 E-value: 8.76e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 4 IIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQLIA 83
Cdd:PRK14180 3 LIDGKSLSKDLKERLATQVQEYKHHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 84 DLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTAL-DMEANIPATPLGVKRLLEHMKIETLGRNAV 162
Cdd:PRK14180 83 QLNNDSSVHAILVQLPLPAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLrDKKCLESCTPKGIMTMLREYGIKTEGAYAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 163 VVGRSKNVSLPMA-ILLHAdgkyatkamDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGI 241
Cdd:PRK14180 163 VVGASNVVGKPVSqLLLNA---------KATVTTCHRFT--TDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17136818 242 NRIKDestgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARK 295
Cdd:PRK14180 232 NHVDG------KIVGDVDFAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQE 279
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-295 |
2.52e-74 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 229.58 E-value: 2.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 1 MAQIIDGKAIAQEVRTQLAHELKGMEAAGyPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQ 80
Cdd:PRK14170 1 MGEIIDGKKLAKEIQEKVTREVAELVKEG-KKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 81 LIADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRN 160
Cdd:PRK14170 80 VVEELNEDKTIHGILVQLPLPEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 161 AVVVGRSKNVSLPMAILLHADgkyatkamDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVG 240
Cdd:PRK14170 160 AVVIGRSNIVGKPVAQLLLNE--------NATVTIAHSRT--KDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVG 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17136818 241 INRikDESTgqfKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARK 295
Cdd:PRK14170 230 MDR--DENN---KLCGDVDFDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-292 |
1.13e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 227.92 E-value: 1.13e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 1 MAQIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQ 80
Cdd:PRK14171 1 MNNIIDGKALANEILADLKLEIQELKSQTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 81 LIADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIG--RTALDmEANIPATPLGVKRLLEHMKIETLG 158
Cdd:PRK14171 81 KINELNLDNEISGIIVQLPLPSSIDKNKILSAVSPSKDIDGFHPLNVGylHSGIS-QGFIPCTALGCLAVIKKYEPNLTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 159 RNAVVVGRSKNVSLPMAILLHADgkyatkamDATVTICHRYTppKELARHCRQADIIVVAVGKPGLITKDMVKPGACVID 238
Cdd:PRK14171 160 KNVVIIGRSNIVGKPLSALLLKE--------NCSVTICHSKT--HNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVID 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17136818 239 VGINRIkdestGQFKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKA 292
Cdd:PRK14171 230 VGINRI-----SGNKIIGDVDFENVKSKVKYITPVPGGIGPMTIAFLLKNTVKA 278
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
33-295 |
3.91e-70 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 218.96 E-value: 3.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 33 PHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQLIADLNKDPQVTGILVQLPVPEHINERTICNA 112
Cdd:PRK14181 27 PGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDPNIHGILVQLPLPKHLDAQAILQA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 113 VDVDKDVDGFNEVNIGRTAL-DMEANIPATPLGVKRLLEHMKIETLGRNAVVVGRSKNVSLPMAILL---HADgkyatka 188
Cdd:PRK14181 107 ISPDKDVDGLHPVNMGKLLLgETDGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIVGKPLAALLmqkHPD------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 189 MDATVTICHryTPPKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGINRIKDESTGQFKLVGDVDFEEVRQVAG 268
Cdd:PRK14181 180 TNATVTLLH--SQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVPAANPKGYILVGDVDFNNVVPKCR 257
|
250 260
....*....|....*....|....*..
gi 17136818 269 HITPVPGGVGPMTVAMLMHNTLKAARK 295
Cdd:PRK14181 258 AITPVPGGVGPMTVAMLMRNTWESYLR 284
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
5-120 |
4.03e-56 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 176.83 E-value: 4.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 5 IDGKAIAQEVRTQLAHELKGMEAAGYpKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQLIAD 84
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKAGGR-KPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDK 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 17136818 85 LNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVD 120
Cdd:pfam00763 80 LNADPSVHGILVQLPLPKHIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
138-294 |
2.10e-22 |
|
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NAD(P) binding domains of methylene-tetrahydrofolate dehydrogenase (m-THF DH) and m-THF DH/cyclohydrolase bifunctional enzymes (m-THF DH/cyclohydrolase). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, mono-functional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express a monofunctional DH. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133451 Cd Length: 140 Bit Score: 90.64 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 138 IPATPLGVKRLLEHMKI------ETL-GRNAVVVGRSKNVSLPMAILLHADGkyatkamdATVTICHRYTPPKELARHcr 210
Cdd:cd05212 1 GPCTPLFVSPVAKAVKEllnkegVRLdGKKVLVVGRSGIVGAPLQCLLQRDG--------ATVYSCDWKTIQLQSKVH-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 211 QADIIVVAVGKPGLITKDMVKPGACVIDVGINRIKDEstgqfklvgdvdfeEVRQVAGHITPVPGGVGPMTVAMLMHNTL 290
Cdd:cd05212 71 DADVVVVGSPKPEKVPTEWIKPGATVINCSPTKLSGD--------------DVKESASLYVPMTGGVGKLTVAMRMQNMV 136
|
....
gi 17136818 291 KAAR 294
Cdd:cd05212 137 RSVR 140
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
116-296 |
8.05e-08 |
|
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of methylene-tetrahydrofolate dehydrogenase (m-THF DH). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. M-THF DH is a component of an unusual monofunctional enzyme; in eukaryotes, m-THF DH is typically found as part of a multifunctional protein. NADP-dependent m-THF DHs in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofunctional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains only the monofunctional DHs from S. cerevisiae and certain bacteria. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133447 [Multi-domain] Cd Length: 197 Bit Score: 51.66 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 116 DKDVDGFNEVNIGRTA-----LDMEAN----IPATPLGVKRLLEHMKI---------ETLGRNAVVVGRSKNVSLPMAIL 177
Cdd:cd01079 2 HKDVEGLSHKYIFNLYhnirfLDPENRkksiLPCTPLAIVKILEFLGIynkilpygnRLYGKTITIINRSEVVGRPLAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136818 178 LHADGKyATKAMDATVTIC-----------HRYTPPKELARHC-RQADIIVVAVGKPGL-ITKDMVKPGACVIDVginri 244
Cdd:cd01079 82 LANDGA-RVYSVDINGIQVftrgesirhekHHVTDEEAMTLDClSQSDVVITGVPSPNYkVPTELLKDGAICINF----- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17136818 245 kdeSTGQFklvgdvDFEEVRQVAGHITPVpggVGPMTVAMLMHNTLKAARKQ 296
Cdd:cd01079 156 ---ASIKN------FEPSVKEKASIYVPS---IGKVTIAMLLRNLLRLYHNQ 195
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
202-241 |
1.66e-05 |
|
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440450 [Multi-domain] Cd Length: 372 Bit Score: 45.77 E-value: 1.66e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 17136818 202 PKELARHCRQADIIVVAVGKPG-----LITKDMV---KPGACVIDVGI 241
Cdd:COG0686 222 PANIEEALKEADLVIGAVLIPGarapkLVTREMVkrmKPGSVIVDVAI 269
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
202-241 |
7.95e-05 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 42.11 E-value: 7.95e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 17136818 202 PKELARHCRQADIIVVAVGKPG-----LITKDMV---KPGACVIDVGI 241
Cdd:smart01002 74 AELLEEAVKEADLVIGAVLIPGakapkLVTREMVksmKPGSVIVDVAA 121
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
198-241 |
1.07e-04 |
|
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.
Pssm-ID: 426165 [Multi-domain] Cd Length: 213 Bit Score: 42.48 E-value: 1.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 17136818 198 RYTPPKELARHCRQADIIVVAVGKPG-----LITKDMV---KPGACVIDVGI 241
Cdd:pfam01262 79 LYSQAELIAEAVKEADLVIGTALIPGakapkLVTREMVksmKPGSVIVDVAI 130
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
202-241 |
4.24e-04 |
|
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.
Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 41.24 E-value: 4.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 17136818 202 PKELARHCRQADIIVVAVGKPG-----LITKDMV---KPGACVIDVGI 241
Cdd:cd05305 222 PANLEEALKEADLVIGAVLIPGakapkLVTEEMVktmKPGSVIVDVAI 269
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
203-238 |
4.26e-03 |
|
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matrix side. DI contains 2 domains in Rossmann-like folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than a classical Rossmann domain.
Pssm-ID: 240629 [Multi-domain] Cd Length: 363 Bit Score: 38.16 E-value: 4.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 17136818 203 KELARHCRQADIIVV--AV-GK--PGLITKDMV---KPGACVID 238
Cdd:cd05304 241 ELLAKHIAEADIVITtaLIpGRkaPKLITKEMVesmKPGSVIVD 284
|
|
| |
